8SW6: Protein Phosphatase 1

Protein Phosphatase 1 in complex with PP1-specific Phosphatase targeting peptide (PhosTAP) version 3. Determined by X-ray diffraction at 1.76 Å resolution. Released 29 May 2024.

Method: X-ray diffraction
Resolution: 1.76 Å
Organism: Homo sapiens
Chains: 4
Atoms: 5,698
Mol. weight: 79.71 kDa
Ligands: MN
Released: 29 May 2024

Explore 8SW6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8SW6 contains 26 α-helices and 40 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 12 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
α-helix	32-48	17
β-strand	52-55	4	1
β-strand	59-62	4	2
β-strand	64	1	3
α-helix	69-79	11
β-strand	87-89	3	2
α-helix	100-113	14
β-strand	118-120	3	2
α-helix	128-131	4
α-helix	136-143	8
α-helix	146-156	11
β-strand	162-165	4	1
β-strand	169-171	3	1
α-helix	183-187	5
α-helix	194-196	3
α-helix	200-206	7
β-strand	208-209	2	4
β-strand	216-218	3	4
β-strand	225-227	3	4
α-helix	229-239	11
β-strand	243-246	4	1
β-strand	255-258	4	1
β-strand	263-266	4	1
β-strand	267	1	3
α-helix	272-274	3
β-strand	280-285	6	2
β-strand	290	1	5
β-strand	291-298	8	2

Chain B: 13 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
α-helix	32-48	17
β-strand	52-55	4	6
β-strand	59-62	4	7
β-strand	64	1	8
α-helix	69-79	11
β-strand	87-89	3	7
α-helix	100-113	14
β-strand	118-120	3	7
α-helix	121-123	3
α-helix	128-131	4
α-helix	136-143	8
α-helix	146-156	11
β-strand	162-165	4	6
β-strand	169-171	3	6
α-helix	183-187	5
α-helix	194-196	3
α-helix	200-206	7
β-strand	208-209	2	9
β-strand	216-218	3	9
β-strand	225-227	3	9
α-helix	229-239	11
β-strand	243-246	4	6
β-strand	255-258	4	6
β-strand	263-266	4	6
β-strand	267	1	8
α-helix	272-274	3
β-strand	280-285	6	7
β-strand	290	1	10
β-strand	291-296	6	7

Chain C: 1 helix, 3 β-strands

Element	Residues	Length	Sheet
β-strand	388	1	1
β-strand	400	1	5
α-helix	404-406	3
β-strand	408-413	6	2

Chain D: 0 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	388	1	6
β-strand	400	1	10
β-strand	408-410	3	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit	A, B	protein	299	Homo sapiens	P62136 (AlphaFold model)
PP1-specific Phosphatase-Targeting Peptide version 3	C, D	protein	43	Homo sapiens

Sequence of entity 1 (A, B), FASTA

>8SW6_1 Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (chains A, B)
GHMGSLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKI
CGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLL
RGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQ
SMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDL
DLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD

Sequence of entity 2 (C, D), FASTA

>8SW6_2 PP1-specific Phosphatase-Targeting Peptide version 3 (chains C, D)
GHMKGILKREKRLRRKNVHWPEEGKLREYFYFELDEAERVNVN

Ligands and cofactors

ID	Name	Formula	Copies
MN	Manganese (II) ion	Mn	4

Water and common crystallization additives (CL, SO4) are not listed.

Primary citation

A protein phosphatase 1 specific phos phatase ta rgeting p eptide (PhosTAP) to identify the PP1 phosphatome. Choy, M.S., Nguyen, H.T., Kumar, G.S. et al. Proc Natl Acad Sci U S A (2024) 121:e2415383121-e2415383121. DOI 10.1073/pnas.2415383121 · PubMed

Other PDB entries of the same protein (UniProt P62136 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6ZEG 1.09 Å, Structure of PP1-IRSp53 chimera [PP1(7-304) + linker (G/S)x9 + IRSp53(449-465)] bound to…
6ZEH 1.3 Å, Structure of PP1-spectrin alpha II chimera [PP1(7-304) + linker (G/S)x9 + spectrin alpha…
6ZEI 1.39 Å, Structure of PP1-IRSp53 S455E chimera [PP1(7-304) + linker (G/S)x9 + IRSp53(449-465)]…
6DNO 1.45 Å, Crystal structure of Protein Phosphatase 1 (PP1) bound to the muscle glycogen-targeting…
4MOV 1.45 Å, 1.45 A Resolution Crystal Structure of Protein Phosphatase 1
6OBR 1.5 Å, PP1 Y134A in complex with Microcystin LR
3E7A 1.63 Å, Crystal Structure of Protein Phosphatase-1 Bound to the natural toxin Nodularin-R
3E7B 1.7 Å, Crystal Structure of Protein Phosphatase-1 Bound to the natural toxin inhibitor Tautomycin
6ZEJ 1.78 Å, Structure of PP1-Phactr1 chimera [PP1(7-304) + linker (SGSGS) + Phactr1(526-580)]
7T0Y 1.8 Å, The Ribosomal RNA Processing 1B Protein Phosphatase-1 Holoenzyme
6OBS 1.8 Å, PP1 Y134K
6OBQ 1.84 Å, PP1 H66K in complex with Microcystin LR

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